Halophilic proteins are stable and function at high salt concentration. Understanding how
these molecules maintain their fold stable and avoid aggregation under harsh conditions is …

This latest edition of the most internationally respected reference in food chemistry for more
than 30 years, Fennema's Food Chemistry once again meets and surpasses the standards …

The amino acid constituents are linked to each other in a linear sequence via substituted
amide bonds. Unlike the glycosidic bonds in polysaccharides and phosphodiester bonds in …

We present a new thermodynamic model to investigate the relative effects of excluded
volume and soft interaction contributions in determining whether a cosolute will either …

An entropic stabilization mechanism has recently gained attention and credibility as the
physical ground for the extra thermal stability of globular proteins from thermophilic …

Cell adhesion to surfaces represents the basis for niche colonization and survival. Here we
establish serial quantification of adhesion forces of different cell types using a single probe …

A theoretical rationalization of the occurrence of cold denaturation for globular proteins was
devised, assuming that the effective size of water molecules depends upon temperature [G …

Understanding how material properties affect hydrophobic interactions—the water-mediated
interactions that drive the association of nonpolar materials—is vital to the design of …

Cononsolvency refers to the experimental finding that poly (N-isopropylacrylamide),
PNIPAM, has a coil conformation in both pure water and pure methanol, at 20° C and 1 atm …

A polypeptide chain can adopt very different conformations, a fundamental distinguishing
feature of which is the water accessible surface area, WASA, that is a measure of the layer …